4WQM
Structure of the toluene 4-monooxygenase NADH oxidoreductase T4moF, K270S K271S variant
Summary for 4WQM
| Entry DOI | 10.2210/pdb4wqm/pdb |
| Descriptor | Toluene-4-monooxygenase electron transfer component, FE2/S2 (INORGANIC) CLUSTER, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, iron-sulfur, ferredoxin-nad reductase, electron-transfer |
| Biological source | Pseudomonas mendocina |
| Total number of polymer chains | 1 |
| Total formula weight | 37714.72 |
| Authors | Acheson, J.F.,Fox, B.G. (deposition date: 2014-10-22, release date: 2015-09-09, Last modification date: 2023-12-27) |
| Primary citation | Acheson, J.F.,Moseson, H.,Fox, B.G. Structure of T4moF, the Toluene 4-Monooxygenase Ferredoxin Oxidoreductase. Biochemistry, 54:5980-5988, 2015 Cited by PubMed Abstract: The 1.6 Å crystal structure of toluene 4-monooxygenase reductase T4moF is reported. The structure includes ferredoxin, flavin, and NADH binding domains. The position of the ferredoxin domain relative to the other two domains represents a new configuration for the iron-sulfur flavoprotein family. Close contacts between the C8 methyl group of FAD and [2Fe-2S] ligand Cys36-O represent a plausible pathway for electron transfer between the redox cofactors. Energy-minimized docking of NADH and calculation of hingelike motions between domains suggest how simple coordinated shifts of residues at the C-terminus of the enzyme could expose the N5 position of FAD for productive interaction with the nicotinamide ring. The domain configuration revealed by the T4moF structure provides an excellent steric and electrostatic match to the obligate electron acceptor, Rieske-type [2Fe-2S] ferredoxin T4moC. Protein-protein docking and energy minimization of the T4moFC complex indicate that T4moF [2Fe-2S] ligand Cys41 and T4moC [2Fe-2S] ligand His67, along with other electrostatic interactions between the protein partners, form the functional electron transfer interface. PubMed: 26309236DOI: 10.1021/acs.biochem.5b00692 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.62 Å) |
Structure validation
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